Correction to article ‘Iron–sulfur biology invades tRNA modification: the case of U34 sulfuration’

Nucleic Acids Research ◽

10.1093/nar/gkab310 ◽

2021 ◽

Author(s):

Jingjing Zhou ◽

Marine Lénon ◽

Jean-Luc Ravanat ◽

Nadia Touati ◽

Christophe Velours ◽

...

Keyword(s):

Trna Modification ◽

Iron Sulfur

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Aqueous iron-thiolate chemistry: relevance to iron-sulfur proteins

10.31274/rtd-180813-12285 ◽

1989 ◽

Author(s):

Mark Thomas Werth

Keyword(s):

Iron Sulfur ◽

Iron Sulfur Proteins ◽

Iron Thiolate

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tRNA modification in the mitochondrion

Reactome - a curated knowledgebase of biological pathways ◽

10.3180/r-hsa-6787450.1 ◽

2015 ◽

Vol 55 ◽

Author(s):

B May

Keyword(s):

Trna Modification

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Faculty Opinions recommendation of The roles of coenzyme A in the pyruvate:ferredoxin oxidoreductase reaction mechanism: rate enhancement of electron transfer from a radical intermediate to an iron-sulfur cluster.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1002479.109611 ◽

2002 ◽

Author(s):

Wolfgang Buckel

Keyword(s):

Electron Transfer ◽

Reaction Mechanism ◽

Coenzyme A ◽

Radical Intermediate ◽

Iron Sulfur Cluster ◽

Rate Enhancement ◽

Sulfur Cluster ◽

Iron Sulfur ◽

Pyruvate:Ferredoxin Oxidoreductase

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Faculty Opinions recommendation of Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1015483.196981 ◽

2003 ◽

Author(s):

Joan Broderick

Keyword(s):

Scaffold Protein ◽

Iron Sulfur Cluster ◽

Sulfur Cluster ◽

Iron Sulfur ◽

Subcellular Compartmentalization

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Faculty Opinions recommendation of The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1029526.345457 ◽

2005 ◽

Author(s):

Joan Broderick

Keyword(s):

Protein Assembly ◽

Iron Sulfur ◽

Late Step ◽

Sulfur Protein ◽

Iron Sulfur Protein

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Faculty Opinions recommendation of The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1033739.387940 ◽

2006 ◽

Author(s):

James Penner-Hahn

Keyword(s):

Binding Motif ◽

Iron Binding ◽

Iron Sulfur Cluster ◽

Sulfur Cluster ◽

Iron Sulfur

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Faculty Opinions recommendation of Discovery of epoxyqueuosine (oQ) reductase reveals parallels between halorespiration and tRNA modification.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.11577956.12633054 ◽

2011 ◽

Author(s):

Squire Booker

Keyword(s):

Trna Modification

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Faculty Opinions recommendation of Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1161670.623249 ◽

2009 ◽

Author(s):

Tom Misteli ◽

Gianluca Pegoraro

Keyword(s):

Mitochondrial Dysfunction ◽

Genome Instability ◽

Nuclear Genome ◽

Iron Sulfur Cluster ◽

Sulfur Cluster ◽

Iron Sulfur

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Faculty Opinions recommendation of The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1164926.625763 ◽

2009 ◽

Author(s):

John Helmann

Keyword(s):

Copper Toxicity ◽

Iron Sulfur Clusters ◽

Iron Sulfur ◽

Intracellular Targets

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Faculty Opinions recommendation of Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.14264957.15779244 ◽

2012 ◽

Author(s):

Rowena Matthews

Keyword(s):

Complex Formation ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein

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